Superoxide, O2•−, is formed in all living organisms that come in contact with air, and,
depending upon its biological context, it may act as a signaling agent, a toxic species, or a …

The discovery of superoxide dismutases (SODs), which convert superoxide radicals to
molecular oxygen and hydrogen peroxide, has been termed the most important discovery of …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

Evolutionary information derived from the large number of available protein sequences and
structures could powerfully guide both analysis and prediction of protein–protein interfaces …

The biocoordination chemistry of the uranyl cation (uranium (VI),[UO2] 2+) is assessed
utilizing data from the Protein Databank, solution thermodynamic data and biochemical …

The dissociation of apo-and metal-bound human copper-zinc superoxide dismutase (SOD1)
dimers induced by the chaotrope guanidine hydrochloride (GdnHCl) or the reductant Tris (2 …

We analyzed subunit interfaces in 315 homodimers with an X-ray structure in the Protein
Data Bank, validated by checking the literature for data that indicate that the proteins are …

The sodC-encoded Mycobacterium tuberculosis superoxide dismutase (SOD) shows high
sequence homology to other members of the copper/zinc-containing SOD family. Its three …

Several bacterial pathogens possess sodC genes that encode periplasmic or membrane-
associated Cu, Zn superoxide dismutases. Since professional phagocytes generate large …

The solution structure of homodimeric Cu2Zn2 superoxide dismutase (SOD) of 306
aminoacids was determined on a 13C, 15N and 70% 2H labeled sample. Two‐thousand …